STRUCTURAL CHARACTERIZATION OF THE DIFFERENT DOMAINS OF THE ALPHA ISOFORM OF
α亚型不同域的结构特征
基本信息
- 批准号:7956812
- 负责人:
- 金额:$ 0.47万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2009
- 资助国家:美国
- 起止时间:2009-08-01 至 2010-07-31
- 项目状态:已结题
- 来源:
- 关键词:Chimeric ProteinsComplexComputer Retrieval of Information on Scientific Projects DatabaseData SetEstrogen ReceptorsEvaluationFundingGrantHumanInstitutionKnowledgeLengthLigand Binding DomainProtein IsoformsProteinsResearchResearch PersonnelResourcesSourceTherapeuticTimeUnited States National Institutes of HealthWorkmaltose-binding proteinmutantnovelscaffoldsmall moleculestructural biologytherapeutic target
项目摘要
This subproject is one of many research subprojects utilizing the
resources provided by a Center grant funded by NIH/NCRR. The subproject and
investigator (PI) may have received primary funding from another NIH source,
and thus could be represented in other CRISP entries. The institution listed is
for the Center, which is not necessarily the institution for the investigator.
This proposal is part of our ongoing structural studies aimed at the characterization of all the domains of the hER, biochemically important mutants of these domains, and evaluation of potential therapeutic targets. We have been working on the structural characterization of the human Estrogen Receptor (hER) ligand binding domain (LBD) complexes with potential therapeutic small molecules since the Spring of 2005. These compounds have encompassed those with novel scaffolds, varying potency and selectivity for the different isoforms of hER. We have recently begun to characterize the other domains of hERalpha (besides the LBD). We have obtained crystals of A though D domains of both the wild type and point mutant proteins expressed as fusion products with the maltose binding protein (MBP). These MBP fusion proteins are soluble and have crystallized in several conditions of our intial screens. This is exciting progress because we have no structural knowledge to date, of the three dimensional organization of the various domains of hER. We need beam time to screen these crystals of various length of hER for diffraction quality, so we can optimize the conditions for better crystals. We also hope to collect a few datasets.
这个子项目是众多研究子项目之一
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Shyamala Rajan其他文献
Shyamala Rajan的其他文献
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STRUCTURAL ANALYSES OF HUMAN ESTROGEN RECEPTOR IN COMPLEX WITH EFFECTOR/REGUL
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- 批准号:
8172017 - 财政年份:2010
- 资助金额:
$ 0.47万 - 项目类别:
STRUCTURAL CHARACTERIZATION OF THE DIFFERENT DOMAINS OF THE ALPHA ISOFORM OF
α亚型不同域的结构特征
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7726020 - 财政年份:2008
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$ 0.47万 - 项目类别:
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